Two novel autophosphorylation sites in the juxtamembrane region of the PDGF alpha-receptor, Tyr-572 and Tyr-574, were identified. A Y572/574F mutant PDGF (alpha)-receptor was generated and stably expressed in porcine aortic endothelial cells. In contrast to the wild-type receptor, the mutant receptor was unable to associate with or activate Src family tyrosine kinases. Tyrosine phosphorylated synthetic peptides representing the juxtamembrane sequence of the receptor dose-dependently inhibited the binding of Src family tyrosine kinases to the autophosphorylated PDGF alpha-receptor. The mutant receptor showed similar PDGF-induced kinase activity and ability to mediate mitogenicity, actin reorganization and chemotaxis as the wild-type receptor. Thus activation of Src family kinases by the PDGF alpha-receptor is not essential for PDGF-induced mitogenicity or actin reorganization.
PDGF alpha-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells
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R. Hooshmand-Rad, K. Yokote, C.H. Heldin, L. Claesson-Welsh; PDGF alpha-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells. J Cell Sci 1 March 1998; 111 (5): 607–614. doi: https://doi.org/10.1242/jcs.111.5.607
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